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Literature summary for 1.11.1.21 extracted from

  • Vlasits, J.; Furtmueller, P.G.; Jakopitsch, C.; Zamocky, M.; Obinger, C.
    Probing hydrogen peroxide oxidation kinetics of wild-type Synechocystis catalase-peroxidase (KatG) and selected variants (2010), Biochim. Biophys. Acta, 1804, 799-805.
    View publication on PubMed
Search for more literature for 1.11.1.21

Protein Variants

Protein Variants Comment Organism
D152S the mutant shows strongly reduced catalase activity Synechocystis sp.
E253Q the mutant shows strongly reduced catalase activity Synechocystis sp.
W122F inactive Synechocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
cyanide
-
 Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2
-
 Synechocystis sp. O2 + H2O
-
 ?

Synonyms

Synonyms Comment Organism
EC 1.11.1.7 formerly Synechocystis sp.
KatG
-
 Synechocystis sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
200
-
 H2O2 mutant enzyme D152S, catalase activity, pH and temperature not specified in the publication Synechocystis sp.
890
-
 H2O2 mutant enzyme E243Q, catalase activity, pH and temperature not specified in the publication Synechocystis sp.
3500
-
 H2O2 wild type enzyme, catalase activity, pH and temperature not specified in the publication Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
heme
-
 Synechocystis sp.